ArticleFEBS open bio2016
Outer-sphere residues influence the catalytic activity of a chalcone synthase from Polygonum cuspidatum.
Article in FEBS open bio, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 7 citations in OpenAlex.
- Review
- New Insights on Cyclization Specificity of Fungal Type III Polyketide Synthase, PKSIIIIndian journal of microbiology · 2018Article
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Authors and funding
4 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
We have previously cloned a chalcone synthase (PcCHS1) from Polygonum cuspidatum and biochemically identified its enzymatic dynamic properties. Here, we found that the outer sphere residues, Q82 and R105, could affect the catalytic activity and product profile of PcCHS1. Both Q82P and R105Q mutations of PcCHS1 could also change the pH dependence activity as well as the product profile of PcCHS1. Moreover, the Q82P/C198F double mutant could rescue the complete loss of enzyme activity caused by the C198F single mutation. Our study demonstrated that these outer-sphere residues of PcCHS1 play important roles both in structural maintenance and enzyme activity.
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